Table 1 X-ray data collection and refinement statistics.
From: Structural basis for catalytically restrictive dynamics of a high-energy enzyme state
P177A-Holo | P177A-Apo | Y171W-Holo | Y171W-Apo | |
|---|---|---|---|---|
Data collection | ||||
Space group | P212121 | C2 | P212121 | C2 |
Cell dimensions | ||||
a, b, c (Å) | 82.57, 72.67, 79.31 | 135.42, 31.53, 52.75 | 82.26, 72.65, 79.48 | 123.57, 31.62, 63.08 |
α, β, γ (°) | 90.0, 90.0, 90.0 | 90.0, 110.65, 90.0 | 90.0, 90.0, 90.0 | 90.0, 114.42, 90.0 |
Resolution (Å) | 27.3–1.70 (1.74–1.70)* | 33.6–2.5 (2.59–2.50) | 41.2–2.10 (2.18–2.10) | 33.8–2.60 (2.67–2.60) |
Rmerge | 0.061 (0.267) | 0.139 (0.345) | 0.091 (0.363) | 0.074 (0.275) |
I/σI | 19.5 (5.0) | 16.57 (5.3) | 32.0 (6.48) | 26.0 (3.7) |
Completeness (%) | 99.4 (96.8) | 98.5 (89.0) | 99.7 (98.1) | 97.5 (82.3) |
Redundancy | 7.1 (4.5) | 5.22 (4.2) | 14.79 (4.88) | 4.2 (2.4) |
Refinement | ||||
Resolution (Å) | 27.0–1.70 | 33.6–2.5 | 41.2–2.10 | 33.8–2.60 |
No. of reflections | 52,850 (3,261) | 7,465 (849) | 28,378 (2,747) | 7,007 (640) |
Rwork | 0.177 (0.310) | 0.191 (0.268) | 0.177 (0.216) | 0.246 (0.303) |
Rfree | 0.211 (0.383) | 0.289 (0.347) | 0.239 (0.286) | 0.309 (0.361) |
No. of atoms | ||||
Protein | 3,406 | 1,654 | 3,431 | 1,652 |
Ligand/ion | 118 | — | 117 | — |
Water | 842 | 150 | 337 | 36 |
B-factors | ||||
Protein | 13.4 | 42.9 | 14.4 | 51.2 |
Ligand/ion | 9.3 | — | 10.2 | — |
Water | 25.2 | 43.2 | 17.4 | 35.9 |
r.m.s.d. | ||||
Bond lengths (Å) | 0.003 | 0.003 | 0.004 | 0.003 |
Bond angles (°) | 0.872 | 0.64 | 0.856 | 0.650 |
